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Database: UniProt
Entry: A0A2K5CPT3_AOTNA
LinkDB: A0A2K5CPT3_AOTNA
Original site: A0A2K5CPT3_AOTNA 
ID   A0A2K5CPT3_AOTNA        Unreviewed;       245 AA.
AC   A0A2K5CPT3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE            EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN   Name=PON3 {ECO:0000313|Ensembl:ENSANAP00000010707.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000010707.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000010707.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC         Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000368,
CC         ECO:0000256|RuleBase:RU368025};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC         + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC         Evidence={ECO:0000256|ARBA:ARBA00000450};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602640-2,
CC         ECO:0000256|RuleBase:RU368025};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC       2, ECO:0000256|RuleBase:RU368025};
CC   -!- SIMILARITY: Belongs to the paraoxonase family.
CC       {ECO:0000256|ARBA:ARBA00008595, ECO:0000256|RuleBase:RU368025}.
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DR   AlphaFoldDB; A0A2K5CPT3; -.
DR   Ensembl; ENSANAT00000028510.1; ENSANAP00000010707.1; ENSANAG00000023332.1.
DR   GeneTree; ENSGT00390000008932; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   PANTHER; PTHR11799:SF14; SERUM PARAOXONASE/LACTONASE 3; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   PRINTS; PR01785; PARAOXONASE.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2, ECO:0000256|RuleBase:RU368025};
KW   Disulfide bond {ECO:0000256|RuleBase:RU368025};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368025}; Hydrolase {ECO:0000256|RuleBase:RU368025};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW   ECO:0000256|RuleBase:RU368025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Signal {ECO:0000256|RuleBase:RU368025}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU368025"
FT   CHAIN           19..245
FT                   /note="Paraoxonase"
FT                   /evidence="ECO:0000256|RuleBase:RU368025"
FT                   /id="PRO_5029942544"
FT   ACT_SITE        114
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
SQ   SEQUENCE   245 AA;  27771 MW;  0449FF6D3BA051B3 CRC64;
     MGKLVALVLL GVSLSLVGER FLEFRERSNA SREVESVEPE NCHLIEEIEN GSEDIDILPS
     GLAFISSGLK YPGLPNFAPN EPGKIFLIDL NEQKPRVQAL EISGGFDKEL FNPHGISIFI
     DKDHTVYLYI VNHPHMKSTV EIFKFEEQHR SLVYLKTTKH ELLKSVNDIV VFGPEQFYAT
     RDCYFTNSFL SLFEMILDLH WTYVLFYSPR EVKVVATGFS SANGITVSAD QKYFASRILC
     LRSPG
//
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